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Prepublished online as a Blood First Edition Paper on February 6, 2003; DOI 10.1182/blood-2002-10-3076. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-10-3076v1 101/11/4628    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Lobo, C.-A. Articles by Lustigman, S. Search for Related Content PubMed PubMed Citation Articles by Lobo, C.-A. Articles by Lustigman, S. Related Collections Red Cells Transfusion Medicine Brief Reports Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 1 June 2003, Vol. 101, No. 11, pp. 4628-4631 RED CELLS Brief report Glycophorin C is the receptor for the Plasmodium falciparum erythrocyte binding ligand PfEBP-2 (baebl) Cheryl-Ann Lobo, Marilis Rodriguez, Marion Reid, and Sara Lustigman From the Department of Molecular Parasitology, The Lindsley Kimball Research Institute, New York Blood Center, New York, NY; and the Department of Immunohematology, The Lindsley Kimball Research Institute, New York Blood Center, New York, NY. We report in this paper that glycophorin C (GPC) is the receptor for PfEBP-2 (baebl, EBA-140), the newly identified erythrocyte binding ligand of Plasmodium falciparum. PfEBP-2 is a member of the Duffy binding–like erythrocyte binding protein (DBL-EBP) family. Although several reports have been published characterizing PfEBP-2, the identity of its erythrocytic receptor was still unknown. Using a combination of enzymatically treated red blood cells (RBCs) and rare, variant RBCs lacking different surface proteins, we have shown that PfEBP-2 does not bind to cells lacking GPC. Additionally, we found that PfEBP-2 binds differentially to variants of GPC lacking exon 2 or exon 3, and determined that the binding domain on GPC is potentially restricted to amino acid residues 14 through 22 within exon 2. Thus PfEBP-2 is involved in a sialic acid–dependent pathway of invasion, which does not involve glycophorin A or glycophorin B and represents a novel route of entry into the RBCs. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: L. Ford, C. A. Lobo, M. Rodriguez, M. G. Zalis, R. L. D. Machado, A. R. B. Rossit, C. E. Cavasini, A. A. R. Couto, P. A. Enyong, and S. Lustigman Differential Antibody Responses to Plasmodium falciparum Invasion Ligand Proteins in Individuals Living in Malaria-Endemic Areas in Brazil and Cameroon Am J Trop Med Hyg, November 1, 2007; 77(5): 977 - 983. [Abstract] [Full Text] [PDF] C. V. Jennings, A. D. Ahouidi, M. Zilversmit, A. K. Bei, J. Rayner, O. Sarr, O. Ndir, D. F. Wirth, S. Mboup, and M. T. Duraisingh Molecular Analysis of Erythrocyte Invasion in Plasmodium falciparum Isolates from Senegal Infect. Immun., July 1, 2007; 75(7): 3531 - 3538. [Abstract] [Full Text] [PDF] D. C. G. Mayer, L. Jiang, R. N. Achur, I. Kakizaki, D. C. Gowda, and L. H. Miller The glycophorin C N-linked glycan is a critical component of the ligand for the Plasmodium falciparum erythrocyte receptor BAEBL PNAS, February 14, 2006; 103(7): 2358 - 2362. [Abstract] [Full Text] [PDF] K. M. VanBuskirk, E. Sevova, and J. H. Adams Conserved residues in the Plasmodium vivax Duffy-binding protein ligand domain are critical for erythrocyte receptor recognition PNAS, November 2, 2004; 101(44): 15754 - 15759. [Abstract] [Full Text] [PDF] A. Cortes, A. Benet, B. M. Cooke, J. W. Barnwell, and J. C. Reeder Ability of Plasmodium falciparum to invade Southeast Asian ovalocytes varies between parasite lines Blood, November 1, 2004; 104(9): 2961 - 2966. [Abstract] [Full Text] [PDF] C.-A. Lobo, K. de Frazao, M. Rodriguez, M. Reid, M. Zalis, and S. Lustigman Invasion Profiles of Brazilian Field Isolates of Plasmodium falciparum: Phenotypic and Genotypic Analyses Infect. Immun., October 1, 2004; 72(10): 5886 - 5891. [Abstract] [Full Text] [PDF] D. C. G. Mayer, J.-B. Mu, O. Kaneko, J. Duan, X.-z. Su, and L. H. Miller Polymorphism in the Plasmodium falciparum erythrocyte-binding ligand JESEBL/EBA-181 alters its receptor specificity PNAS, February 24, 2004; 101(8): 2518 - 2523. [Abstract] [Full Text] [PDF] X. Li, H. Chen, T. H. Oo, T. M. Daly, L. W. Bergman, S.-C. Liu, A. H. Chishti, and S. S. Oh A Co-ligand Complex Anchors Plasmodium falciparum Merozoites to the Erythrocyte Invasion Receptor Band 3 J. Biol. Chem., February 13, 2004; 279(7): 5765 - 5771. [Abstract] [Full Text] [PDF] D. Gaur, J. R. Storry, M. E. Reid, J. W. Barnwell, and L. H. Miller Plasmodium falciparum Is Able To Invade Erythrocytes through a Trypsin-Resistant Pathway Independent of Glycophorin B Infect. Immun., December 1, 2003; 71(12): 6742 - 6746. [Abstract] [Full Text] [PDF]

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